Award Abstract #0216469
Acquisition of Proteomics Equipment for Researchers at HSPH

NSF Org:	DBI Division of Biological Infrastructure
Initial Amendment Date:	June 11, 2002
Latest Amendment Date:	June 11, 2002
Award Number:	0216469
Award Instrument:	Standard Grant
Program Manager:	Robyn E. Hannigan DBI Division of Biological Infrastructure BIO Directorate for Biological Sciences
Start Date:	June 1, 2002
Expires:	May 31, 2005 (Estimated)
Awarded Amount to Date:	$267245
Investigator(s):	Dieter Wolf dwolf@burnham.org (Principal Investigator) Bruce Demple (Co-Principal Investigator) Marianne Wessling-Resnick (Co-Principal Investigator) dyann wirth (Co-Principal Investigator)
Sponsor:	Harvard University 1350 MASSACHUSETTS AVE Cambridge, MA 02138 617/495-5501
NSF Program(s):	MAJOR RESEARCH INSTRUMENTATION
Field Application(s):
Program Reference Code(s):	BIOT, 9184
Program Element Code(s):	1189

ABSTRACT

A grant has been awarded to the Harvard School of Public Health (HSPH) under the direction of Dr. Dieter Wolf to purchase instrumentation which will open new opportunities in the emerging field of system-wide analysis of protein expression and function ("proteomics"). A detailed understanding of the information contained within the many sequenced genomes available in public databases today requires state-of-the-art means of analyzing quantitative and qualitative differences in protein expression and function in a high-throughput format. Peptide mass spectrometry is a relatively new technology that is ideal for these applications and is widely expected to remain the most important core technology of proteomics research for many years to come.

There are two major areas of proteomics research that are addressed with this equipment: 1. protein expression profiling, and 2. identification of protein assemblies purified from complex samples. The research activities enabled by this NSF grant make extensive use of these applications in order to answer major questions in basic biology. The projects use samples derived from organisms across the evolutionary ladder. The scope of research activities is wide-ranging, and includes large scale analysis of the ubiquitin-dependent proteolysis system, analyzing determinants of cellular responses to radicals and oxidative stress, determining factors controlling membrane transport of metals and peptide growth factors, analyzing signaling and transcriptional activation pathways in cell lineage determination, determining protein interactions involved in establishing cell polarity, and many others.

The grant awarded by NSF provides funds for the acquisition of a combined liquid chromatography tandem mass spectrometer system (LC/MS/MS). This instrument adds an essential component of modern proteomics technology to preexisting tools HSPH has committed to this initiative by enabling rapid and highly accurate protein identification from diverse biological samples. The mass spectrometer is integrated with a high performance liquid chromatography system required for sample fractionation. Sophisticated software assists in protein identification and database searching.

Apart from major scientific advances through proteomics technology, the main impact of this grant lies with the enhancement of the training environment at HSPH. The new research instrumentation provides students and postgraduates with hands-on experience in cutting edge proteomics technology, thereby optimally preparing them for the demanding mission of prevailing in the rapidly changing landscape of the post-genomic era. Through the Minority Internship Program administered by the Division of Biological Sciences at HSPH underrepresented groups will be actively recruited to the burgeoning filed of proteomics research.

PUBLICATIONS PRODUCED AS A RESULT OF THIS RESEARCH

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Doud, M.K., Schmidt, M.W., Hines, D., Naumann, C., Kocourek, A., Kashani-Poor, N., Zeidler, R., Wolf, D.A..  "Rapid prefractionation of complex protein lysates with centrifugal membrane adsorber units improves the resolving power of 2D-PAGE-based proteome analysis.,"  BMC Genomics,  v.5,  2004,  p. 25.

Johannsen E., M. Luftig, M.R. Chase, S. Weicksel, E. Cahir-McFarland, D. Illanes, D. Sarracino, and E. Kieff.  "Proteins of purified Epstein-Barr virus,"  Proc Natl Acad Sci U S A,  v.101,  2004,  p. 16286.

Zhou, C., Arslan, F., Wee, S., Krishnan, S., Oliva, A., Leatherwood, J., Wolf, D.A..  "PCI proteins eIF3e and eIF3m define distinct translation initiation factor 3 complexes,"  BMC Biology,  v.3,  2005,  p. 14.


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